Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold.
The structure of an FF domain from human HYPA/FBP11.,Allen M, Friedler A, Schon O, Bycroft M J Mol Biol. 2002 Oct 25;323(3):411-6. PMID:12381297[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Allen M, Friedler A, Schon O, Bycroft M. The structure of an FF domain from human HYPA/FBP11. J Mol Biol. 2002 Oct 25;323(3):411-6. PMID:12381297
